5fim: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The ~~entry~~ 5fim is ~~ON HOLD until Paper~~ Publication

==The structure of Kbp.K from E. coli==

== Structural highlights ==

<table><tr><td colspan='2'>[[5fim]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIM FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fim OCA], [http://pdbe.org/5fim PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fim RCSB], [http://www.ebi.ac.uk/pdbsum/5fim PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Escherichia coli possesses a number of specific K(+) influx and efflux systems that maintain an appropriate intracellular K(+) concentration. Although regulatory mechanisms have been identified for a number of these transport systems, the exact mechanism through which K(+) concentration is sensed in the cell remains unknown. In this work we show that Kbp (K(+) binding protein, formerly YgaU), a soluble 16-kDa cytoplasmic protein from Escherichia coli, is a highly specific K(+) binding protein and is required for normal growth in the presence of high levels of external K(+). Kbp binds a single potassium ion with high specificity over Na(+) and other metal ions found in biological systems, although, in common with K(+) transporters, it also binds Rb(+) and Cs(+). Dissection of the K(+) binding determinants of Kbp suggests a mechanism through which Kbp is able to sense changes in K(+) concentration over the relevant range of intracellular K(+) concentrations.

~~Authors: SMITH~~, B.O., ~~ASHRAF~~, K.U., ~~WALKER, D~~.

The Potassium Binding Protein Kbp Is a Cytoplasmic Potassium Sensor.,Ashraf KU, Josts I, Mosbahi K, Kelly SM, Byron O, Smith BO, Walker D Structure. 2016 May 3;24(5):741-9. doi: 10.1016/j.str.2016.03.017. Epub 2016 Apr , 21. PMID:27112601<ref>PMID:27112601</ref>

~~Description: The structure~~ of ~~Kbp~~.K ~~from E. coli~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Ashraf, K U]]

[[Category: Smith, B O]]

[[Category: Walker, D]]

[[Category: ~~Smith, B.O~~]]

[[Category: Potassium binding]]

[[Category: ~~Ashraf, K.U~~]]

[[Category: Unknown function]]

[[Category: Ygau]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5fim is ON HOLD  until Paper Publication
+==The structure of Kbp.K from E. coli==
+<StructureSection load='5fim' size='340' side='right' caption='[[5fim]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5fim]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIM FirstGlance]. <br>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fim OCA], [http://pdbe.org/5fim PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fim RCSB], [http://www.ebi.ac.uk/pdbsum/5fim PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Escherichia coli possesses a number of specific K(+) influx and efflux systems that maintain an appropriate intracellular K(+) concentration. Although regulatory mechanisms have been identified for a number of these transport systems, the exact mechanism through which K(+) concentration is sensed in the cell remains unknown. In this work we show that Kbp (K(+) binding protein, formerly YgaU), a soluble 16-kDa cytoplasmic protein from Escherichia coli, is a highly specific K(+) binding protein and is required for normal growth in the presence of high levels of external K(+). Kbp binds a single potassium ion with high specificity over Na(+) and other metal ions found in biological systems, although, in common with K(+) transporters, it also binds Rb(+) and Cs(+). Dissection of the K(+) binding determinants of Kbp suggests a mechanism through which Kbp is able to sense changes in K(+) concentration over the relevant range of intracellular K(+) concentrations.
-Authors: SMITH, B.O., ASHRAF, K.U., WALKER, D.
+The Potassium Binding Protein Kbp Is a Cytoplasmic Potassium Sensor.,Ashraf KU, Josts I, Mosbahi K, Kelly SM, Byron O, Smith BO, Walker D Structure. 2016 May 3;24(5):741-9. doi: 10.1016/j.str.2016.03.017. Epub 2016 Apr , 21. PMID:27112601<ref>PMID:27112601</ref>
-Description: The structure of Kbp.K from E. coli
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5fim" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Ashraf, K U]]
+[[Category: Smith, B O]]
 [[Category: Walker, D]]
-[[Category: Smith, B.O]]
+[[Category: Potassium binding]]
-[[Category: Ashraf, K.U]]
+[[Category: Unknown function]]
+[[Category: Ygau]]